STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
valSvaline--tRNA ligase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 1 subfamily. (878 aa)    
Predicted Functional Partners:
KXK64779.1
Protein FolC; KEGG: cth:Cthe_1384 1.6e-50 FolC bifunctional protein; K11754 dihydrofolate synthase / folylpolyglutamate synthase; Psort location: Cytoplasmic, score: 9.97.
  
  
 0.879
guaA
GMP synthase domain protein; Catalyzes the synthesis of GMP from XMP.
  
  
 0.868
thrS
threonine--tRNA ligase; Catalyzes the attachment of threonine to tRNA(Thr) in a two- step reaction: L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr).
 
  
 0.840
hisS
histidine--tRNA ligase; KEGG: tte:TTE1230 7.5e-140 hisS; histidyl-tRNA synthetase K01892; Psort location: Cytoplasmic, score: 10.00.
 
 
 0.831
leuS
leucine--tRNA ligase; KEGG: txy:Thexy_2006 0. leucyl-tRNA synthetase K01869; Psort location: Cytoplasmic, score: 9.97; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
0.828
argS
arginine--tRNA ligase; KEGG: cst:CLOST_1149 1.2e-166 argS; arginyl-tRNA synthetase 2 K01887; Psort location: Cytoplasmic, score: 9.97.
 
  
 0.821
ileS
isoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as 'pretransfer' editing and involves the hydrolysis of activated Val-AMP. The other activity is designated 'posttransfer' editing and involves deacylation of mischarged Val-tRNA(Ile). Belongs to the class-I aminoacyl-tRNA synthetase family. IleS type 2 subfamily.
  
 
0.816
ispH
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. Belongs to the IspH family.
  
  
 0.797
serS
serine--tRNA ligase; Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L- seryl-tRNA(Sec), which will be further converted into selenocysteinyl- tRNA(Sec).
  
  
 0.785
alaS
alanine--tRNA ligase; Catalyzes the attachment of alanine to tRNA(Ala) in a two- step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
 
  
 0.773
Your Current Organism:
Christensenella minuta
NCBI taxonomy Id: 626937
Other names: C. minuta, Catabacter sp. YIT 12065, Christensenella minuta Morotomi et al. 2012, DSM 22607, JCM 16072, YIT 12065
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